Protein adsorption onto diethylaminoethyl dextran modified anion exchanger: Effect of ionic strength and column behavior
Separation Science and Engineering|Updated:2026-01-06
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Protein adsorption onto diethylaminoethyl dextran modified anion exchanger: Effect of ionic strength and column behavior
Protein adsorption onto diethylaminoethyl dextran modified anion exchanger: Effect of ionic strength and column behavior
中国化学工程学报(英文版)2018年26卷第2期 页码:259-267
Affiliations:
Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University,Tianjin,China,300072
Our previous studies on bovine serum albumin (BSA) adsorption to diethylaminoethyl dextran (DEAE dextran
DexD
grafting-ligand) and DEAE (D
surface-ligand) modified Sepharose FF resins found that all the grafted resins (FF-DexD and FF-D-DexD) exhibited extremely fast uptake rate (effective diffusivity
D
e
D
e
/D
0
N 1.4)
which was six times greater than the ungrafted resins (D
e
/D
0
b 0.3). In this work
the influence of ionic strength (IS) on 6 typical DEAE dextran-grafted resins was investigated. Bath adsorption equilibria and kinetics
breakthrough
and linear gradient elution experiments were conducted. Commercial DEAE Sepharose FF was used for comparison. It is found that protein adsorption capacities on DEAE dextran-FF resins and the commercial resin decreased with increasing IS
but DEAE dextran-FF resins exhibited much higher capacity sensitivity to salt concentration. Besides
steeper decrease of adsorption capacities could be obtained at higher graftingligand or surface-ligand density. It is worth noting that the facilitating role of surface-ligand to the "chain delivery" effect was weakened after adding sal
t
leading to the less improvement in uptake rate by increasing surface-ligand density at higher IS. Although the uptake rates of the DEAE dextran-FF resins increased first and then decreased with increasing IS
they kept the extremely high level of D
e
values (D
e
/D
0
N 1.1) at the their working/binding IS range. Moreover
the DEAE dextran-FF resin displayed much higher adsorption capacities and D
e
values than commercial ungrafted resin in their working condition. Furthermore
the column results of DEAE dextran-FF resins presented higher dynamic binding capacities than and similar elution ISs with DEAE Sepharose FF to achieve similar (or even higher) recoveries suggest the excellent chromatographic column performance of the DEAE dextran-FF resins. Finally
both high recovery and purity of BSA and γ-globulin could be easily achieved using the typical DEAE dextran-FF column
FF-D60-DexD160
to separate their binary mixtures
by step gradient elution. The research has provided new insights into the practical application of the series of DEAE-dextran grafted resins in protein chromatography and proved their superiority.
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